Reviewed, UniProtKB/Swiss-Prot Q9U8B8 (DYR_HELVI)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase
    EC=1.5.1.3

Gene names

Name:

DHFR

Organism

Heliothis virescens (Tobacco budworm moth)

Taxonomic identifier

7102 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Noctuoidea › Noctuidae › Heliothinae › Heliothis

Protein attributes

Sequence length	185 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH. UniProtKB P28019
Enzyme regulation	Activated by dithiothreitol and p-chloromercuribenzoate. Inhibited by trimethoprim, methotrexate, sodium tetrathionate and hydroxymercuribenzoate. Ref.1
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Miscellaneous	The reaction catalyzed by this enzyme represents an essential step for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.
Sequence similarities	Belongs to the dihydrofolate reductase family. UniProtKB P28019 Contains 1 DHFR (dihydrofolate reductase) domain.

Ontologies

Keywords
Biological process	One-carbon metabolism
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glycine biosynthetic process Inferred from electronic annotation. Source: InterPro nucleotide biosynthetic process Inferred from electronic annotation. Source: InterPro one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NADP or NADPH binding Inferred from electronic annotation. Source: InterPro dihydrofolate reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 185	185	Dihydrofolate reductase		PRO_0000186371
Regions
	Domain	5 – 184	180	DHFR
Experimental info
	Sequence conflict	5	1	K → L AA sequence Ref.1
	Sequence conflict	7	1	N → D AA sequence Ref.1
	Sequence conflict	11 – 13	3	AAC → IFD AA sequence Ref.1
	Sequence conflict	15	1	N → D AA sequence Ref.1
	Sequence conflict	21	1	N → D AA sequence Ref.1
	Sequence conflict	158	1	H → Q AA sequence Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9U8B8-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 9B8C0E50ED175812	FASTA	185	21,089
	10 20 30 40 50 60 MSQVKLNLIA AACDNMGIGV NGALPWRLKK EMAYFTTMTS KVSEPTKVNA VIMGRRTWDC 70 80 90 100 110 120 IPDKYRPLQD RVNIVLTHNV DSVKENVPEG VMVFPGLDEA IKYIEGREDI ESTWVIGGSS 130 140 150 160 170 180 IYRAAMTHPN CGKIYLTEIQ KSFDCDTFFP NIDKQQFHLV DEEQIPGEKQ VEGNISYYFR VYKKL

References

[1]

"Tobacco budworm dihydrofolate reductase is a promising target for insecticide discovery." Walker V.K., Tyshenko M.G., Kuiper M.J., Dargar R.V., Yuhas D.A., Cruickshank P.A., Chaguturu R. Eur. J. Biochem. 267:394-403(2000) [PubMed: 10632709] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 3-22; 32-38; 143-149; 153-159 AND 170-175, ENZYME REGULATION. Tissue: Larva.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF104106 mRNA. Translation: AAF04459.1.
3D structure databases
HSSP	HSSP built from PDB template 1KMV based on UniProtKB P00374.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.5.1.3. 118771.
Family and domain databases
InterPro	IPR012259. DHFR. IPR001796. DHFR_reg. IPR017925. Dihydrofolate_reductase_CS. [Graphical view]
PANTHER	PTHR11549:SF1. DHFR. 1 hit.
Pfam	PF00186. DHFR_1. 1 hit. [Graphical view]
PRINTS	PR00070. DHFR.
PROSITE	PS00075. DHFR_1. 1 hit. PS51330. DHFR_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DYR_HELVI

Accession

Primary (citable) accession number: Q9U8B8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	May 1, 2000
Last modified:	September 22, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)